The enzymatic digestion of elastin at acidic pH.
The enzymatic degradation of insoluble elastin has been studied at several pH values using purified pepsin and cathepsin D, and neutrophil extracts. Pepsin degraded elastin throughout the pH range of 1.2-4.0 with the optimum pH below 2.0. Molecular sieve chromatography and gel electrophoresis indicated that a spectrum of molecular weight degradation products was produced. The degradation by pepsin was inhibited by sodium dodecyl sulfate (SDS), NaCl and pepstatin. Cathepsin D, which, like pepsin, degrades hemoglobin at acid pH and is inhibited by pepstatin, had no activity against insoluble elastin in the pH range of 3.2-7.2. Extracts of neutrophils degraded elastin above pH 4.0. The pH profile of elastin degradation by neutrophil extracts generally followed that of purified human leukocyte elastase. Our results suggest that during alimentation or pulmonary aspiration of gastric contents, extracellular elastin may be digested by gastric juice at acid pH. Inflammatory cells would not appear to be capable of contributing to such actions until local pH approaches neutrality. Cathepsin D, a major constituent of inflammatory cells, does not digest all types of connective tissue proteins.
D000813:Anilides / Q000378:metabolism; D000818:Animals; D002402:Cathepsin D; D002403:Cathepsins / Q000378:metabolism*; D002417:Cattle; D002850:Chromatography, Gel; D004549:Elastin / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D008706:Methemoglobin / Q000378:metabolism; D009504:Neutrophils / Q000502:physiology*; D009842:Oligopeptides / Q000378:metabolism; D010434:Pepsin A / Q000378:metabolism*; D013552:Swine
D000813:Anilides; D009842:Oligopeptides; C015516:succinyl-trialanine-4-nitroanilide; D004549:Elastin; D008706:Methemoglobin; D002403:Cathepsins; D010434:Pepsin A; D002402:Cathepsin D